Beta-sandwich or β-sandwich domains consisting of 80 to 350 amino acids occur commonly in proteins. They are characterized by two opposing antiparallel beta sheets (β-sheets).[1] The number of strands found in such domains may differ from one protein to another. β-sandwich domains are subdivided in a variety of different folds. The immunoglobulin-type fold found in antibodies (Ig-fold) consists of a sandwich arrangement of 7-9 antiparallel β-strands arranged in two β-sheets with a Greek-key topology.[2] The Greek-key topology is also found in Human Transthyretin. The jelly-roll topology is found in carbohydrate binding proteins such as concanavalin A and various lectins, in the collagen binding domain of Staphylococcus aureus Adhesin and in modules that bind fibronectin as found in Tenascin (Third Fibronectin Type III Repeat). The L-type lectin domain is a variation of the jelly roll fold. The C2 domain in its typical version (PKC-C2) is a β-sandwich composed of 8 beta-strands (β-strands).
References
edit- ^ Kister, A. E.; Fokas, A. S.; Papatheodorou, T. S.; Gelfand, I. M. (2006). "Strict rules determine arrangements of strands in sandwich proteins". PNAS. 103 (11): 4107–4110. Bibcode:2006PNAS..103.4107K. doi:10.1073/pnas.0510747103. PMC 1449654. PMID 16537492.
- ^ Bokhove, Marcel; Jovine, Luca (2018-01-01), Litscher, Eveline S.; Wassarman, Paul M. (eds.), "Chapter Thirteen - Structure of Zona Pellucida Module Proteins", Current Topics in Developmental Biology, Extracellular Matrix and Egg Coats, 130, Academic Press: 413–442, doi:10.1016/bs.ctdb.2018.02.007, PMID 29853186, retrieved 2020-12-15
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